S38A9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: S38A9_HUMAN
• UniProt AC: Q8NBW4
• Protein Name: Sodium-coupled neutral amino acid transporter 9 {ECO:0000305}
• Gene Name: SLC38A9 {ECO:0000312|HGNC:HGNC:26907}
• Organism: Homo sapiens (Human).
• Sequence Length: 561
• Subcellular Localization: Lysosome membrane ; Multi-pass membrane protein . Late endosome membrane ; Multi-pass membrane protein .
• Protein Description: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acids. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. [PubMed: 25561175]
• Protein Sequence: MANMNSDSRHLGTSEVDHERDPGPMNIQFEPSDLRSKRPFCIEPTNIVNVNHVIQRVSDHASAMNKRIHYYSRLTTPADKALIAPDHVVPAPEECYVYSPLGSAYKLQSYTEGYGKNTSLVTIFMIWNTMMGTSILSIPWGIKQAGFTTGMCVIILMGLLTLYCCYRVVKSRTMMFSLDTTSWEYPDVCRHYFGSFGQWSSLLFSLVSLIGAMIVYWVLMSNFLFNTGKFIFNFIHHINDTDTILSTNNSNPVICPSAGSGGHPDNSSMIFYANDTGAQQFEKWWDKSRTVPFYLVGLLLPLLNFKSPSFFSKFNILGTVSVLYLIFLVTFKAVRLGFHLEFHWFIPTEFFVPEIRFQFPQLTGVLTLAFFIHNCIITLLKNNKKQENNVRDLCIAYMLVTLTYLYIGVLVFASFPSPPLSKDCIEQNFLDNFPSSDTLSFIARIFLLFQMMTVYPLLGYLARVQLLGHIFGDIYPSIFHVLILNLIIVGAGVIMACFYPNIGGIIRYSGAACGLAFVFIYPSLIYIISLHQEERLTWPKLIFHVFIIILGVANLIVQFFM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MANMNSDSRHLGT --CCCCCCCCCCCCC	26.62	23401153
8	Phosphorylation	MANMNSDSRHLGTSE CCCCCCCCCCCCCCC	22.78	24043423
13	Phosphorylation	SDSRHLGTSEVDHER CCCCCCCCCCCCCCC	28.24	29255136
14	Phosphorylation	DSRHLGTSEVDHERD CCCCCCCCCCCCCCC	33.55	29255136
32	Phosphorylation	MNIQFEPSDLRSKRP CCEECCCHHHHCCCC	41.92	24719451
36	Phosphorylation	FEPSDLRSKRPFCIE CCCHHHHCCCCCEEC	40.07	24719451
37	Ubiquitination	EPSDLRSKRPFCIEP CCHHHHCCCCCEECC	58.62	-
66	Ubiquitination	DHASAMNKRIHYYSR HHHHHHHHHHHHHHC	39.38	-
70	Phosphorylation	AMNKRIHYYSRLTTP HHHHHHHHHHCCCCH	10.77	17053785
71	Phosphorylation	MNKRIHYYSRLTTPA HHHHHHHHHCCCCHH	3.52	17053785
72	Phosphorylation	NKRIHYYSRLTTPAD HHHHHHHHCCCCHHH	17.41	-
80	Ubiquitination	RLTTPADKALIAPDH CCCCHHHHHCCCCCC	47.39	-
96	Phosphorylation	VPAPEECYVYSPLGS CCCCCCCEEECCCCC	13.00	26356563
98	Phosphorylation	APEECYVYSPLGSAY CCCCCEEECCCCCEE	4.33	25884760
99	Phosphorylation	PEECYVYSPLGSAYK CCCCEEECCCCCEEE	12.01	26356563
103	Phosphorylation	YVYSPLGSAYKLQSY EEECCCCCEEEEEHH	35.79	28122231
105	Phosphorylation	YSPLGSAYKLQSYTE ECCCCCEEEEEHHHC	17.58	17053785
106	Ubiquitination	SPLGSAYKLQSYTEG CCCCCEEEEEHHHCC	39.50	-
118	Phosphorylation	TEGYGKNTSLVTIFM HCCCCCCHHHHHHHH	27.24	27732954
119	Phosphorylation	EGYGKNTSLVTIFMI CCCCCCHHHHHHHHH	30.18	27732954
122	Phosphorylation	GKNTSLVTIFMIWNT CCCHHHHHHHHHHHH	17.50	27732954
129	Phosphorylation	TIFMIWNTMMGTSIL HHHHHHHHHCCCHHH	8.11	27732954
133	Phosphorylation	IWNTMMGTSILSIPW HHHHHCCCHHHCCCC	8.49	27732954
134	Phosphorylation	WNTMMGTSILSIPWG HHHHCCCHHHCCCCC	18.79	27732954
137	Phosphorylation	MMGTSILSIPWGIKQ HCCCHHHCCCCCCHH	25.57	27732954
239	N-linked_Glycosylation	FNFIHHINDTDTILS HHHHHHCCCCCCCCC	41.60	UniProtKB CARBOHYD
248	N-linked_Glycosylation	TDTILSTNNSNPVIC CCCCCCCCCCCCEEC	46.70	UniProtKB CARBOHYD
266	N-linked_Glycosylation	GSGGHPDNSSMIFYA CCCCCCCCCCEEEEE	40.20	UniProtKB CARBOHYD
274	N-linked_Glycosylation	SSMIFYANDTGAQQF CCEEEEECCHHCHHH	35.68	UniProtKB CARBOHYD
307	Phosphorylation	LPLLNFKSPSFFSKF HHHHCCCCHHHHHCC	22.95	19835603
309	Phosphorylation	LLNFKSPSFFSKFNI HHCCCCHHHHHCCCH	46.12	19835603
312	Phosphorylation	FKSPSFFSKFNILGT CCCHHHHHCCCHHHH	34.04	19835603
321	Phosphorylation	FNILGTVSVLYLIFL CCHHHHHHHHHHHHH	13.27	19835603
324	Phosphorylation	LGTVSVLYLIFLVTF HHHHHHHHHHHHHHH	8.80	19835603
397	Phosphorylation	VRDLCIAYMLVTLTY HHHHHHHHHHHHHHH	3.23	24043423
401	Phosphorylation	CIAYMLVTLTYLYIG HHHHHHHHHHHHHHH	14.93	24043423
403	Phosphorylation	AYMLVTLTYLYIGVL HHHHHHHHHHHHHHH	11.34	24043423
404	Phosphorylation	YMLVTLTYLYIGVLV HHHHHHHHHHHHHHH	10.71	24043423
406	Phosphorylation	LVTLTYLYIGVLVFA HHHHHHHHHHHHHHH	5.80	24043423
414	Phosphorylation	IGVLVFASFPSPPLS HHHHHHHCCCCCCCC	26.65	24043423
417	Phosphorylation	LVFASFPSPPLSKDC HHHHCCCCCCCCHHH	36.82	24043423
421	Phosphorylation	SFPSPPLSKDCIEQN CCCCCCCCHHHHHHC	32.02	24043423
537	Phosphorylation	LHQEERLTWPKLIFH HCHHHCCCHHHHHHH	46.04	19413330

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of S38A9_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of S38A9_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of S38A9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LTOR1_HUMAN	LAMTOR1	physical	25567906
LTOR2_HUMAN	LAMTOR2	physical	25567906
RRAGC_HUMAN	RRAGC	physical	25567906
RRAGA_HUMAN	RRAGA	physical	25567906
VA0D1_HUMAN	ATP6V0D1	physical	25567906
VATB2_HUMAN	ATP6V1B2	physical	25567906

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70; TYR-71 AND TYR-105,AND MASS SPECTROMETRY.
PubMed: 17053785